EC Number   |
Recommended Name |
Application |
|---|
   3.1.1.76 | poly(3-hydroxyoctanoate) depolymerase |
degradation |
enzyme is able to degrade functionalized polyhydroxyalkanoate polymers containing thioester groups in the side chain, releasing functional thioester-based monomers and oligomers |
| 3.1.1.88 | pyrethroid hydrolase |
degradation |
the enzyme can efficiently hydrolyze a wide range of synthetic pyrethroids including fenpropathrin, permethrin, cypermethrin, cyhalothrin, deltamethrin and bifenthrin, which makes it a potential candidate for the detoxification of pyrethroids for the purpose of biodegradation |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
a dual enzyme system consisting of the polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 can be employed for the hydrolysis of PET films at 60°C, resulting in an increased amount of soluble products with a lower proportion of mono-(2-hydroxyethyl)terephthalate in the presence of the immobilized TfCa |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
a dual enzyme system consisting of the polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 can be employed for the hydrolysis of PET films at 60°C, resulting in an increased amount of soluble products with a lower proportion of mono-(2-hydroxyethyl)terephthalate in the presence of the immobilized TfCa. The dual enzyme system with LC-cutinase produces a 2.4fold higher amount of degradation products compared to Thermobifida fusca enzyme Cut2 after a reaction time of 24 h |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
at 50°C, a maximum hydrolysis rate for poly(ethylene terephthalate) nanoparticles of 0.0033 per min is determined with 80 microg/ml of Tcur_1278. With 50 microg/ml of Tcur_1278, the hydrolysis rate increases 1.8fold at 55°C and 2.6fold at 60°C |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
at 50°C, a maximum hydrolysis rate of poly(ethylene terephthalate) nanoparticles of 0.0059 per min is determined with 20 microg/ml of Tcur_0390 |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
biodegradability of PET is mainly influenced by the mobility of the polyester chains, which determine the affinity and accessibility of the ester bonds to the enzyme. The hydrolysis rates of enzymatic PET degradation are predominantly controlled by the efficient substrate adsorption rather than by the hydrolysis of the ester bonds. Nanoparticles prepared from PET samples of different crystallinity show a high proportion of amorphous domains and thus in the corresponding biodegradability |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is was considerably active against PET film at low temperatures |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
exchange of amino acid residues of TfCut2 involved in substrate binding with those present in LC-cutinase, UniProt ID G9BY57, from an uncultured bacterium, leads to enzyme variants with increased PET hydrolytic activity at 65°C. Variant causes a weight loss of PET films of more than 42% after 50 h of hydrolysis, corresponding to a 2.7fold increase compared to the wild type enzyme |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
mutant D204C/E253C/D174R causes a weight loss of PET films of 25.0% at 70°C after a reaction time of 48 h, compared to 0.3% for wild-type |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
the thermostability of the polyester hydrolase is sufficient to degrade semi-crystalline PET films at 65°C in the presence of 10 mM Ca2+ and 10 mM Mg2+ resulting in weight losses of up to 12.9% after a reaction time of 48 h |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
a dual enzyme system composed of a polyester hydrolase and a carboxylesterase enhances the biocatalytic degradation of polyethylene terephthalate films. Since the enzymatic PET hydrolysis is inhibited by the degradation intermediate 4-[(2-hydroxyethoxy)carbonyl]benzoate, a dual enzyme system consisting of a polyester hydrolase and the immobilized carboxylesterase TfCa from Thermobifida fusca KW3 is employed for the hydrolysis of PET films at 60°C. HPLC analysis of the reaction products obtained after 24 h of hydrolysis shows an increased amount of soluble products with a lower proportion of 4-[(2-hydroxyethoxy)carbonyl]benzoate in the presence of the immobilized carboxylesterase TfCa. The results indicate a continuous hydrolysis of the inhibitory 4-[(2-hydroxyethoxy)carbonyl]benzoate by the immobilized carboxylesterase TfCa and demonstrate its advantage as a second biocatalyst in combination with a polyester hydrolase for an efficient degradation oft PET films |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
bioconversion of plastics |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
due to its low structural stability and solubility, it is difficult to apply standard laboratory-level Ideonella sakaiensis PETase expression and purification procedures in industry. To overcome this difficulty, the expression of IsPETase can be improved by using a secretion system. The extracellular enzyme is successfully produced using pET22b-SPMalE:IsPETase and pET22b-SPLamB:IsPETase expression systems. The secreted IsPETase has PET-degradation activity. The work will be used for development of a new Escherichia coli strain capable of degrading and assimilating PET in its culture medium |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
enzymatic degradation of poly(ethylene terephthalate) (PET) is promising because this process is safer than conventional industrial approaches. Acceleration of enzymatic degradation of poly(ethylene terephthalate) is reached by surface coating with anionic surfactants |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
Tat-independent secretion of polyethylene terephthalate hydrolase PETase in Bacillus subtilis 168 mediated by its native signal peptide. Widespread utilization of polyethylene terephthalate (PET) has caused critical environmental pollution. The enzymatic degradation of PET is a promising solution to this problem. PETase, which exhibits much higher PET hydrolytic activity than other enzymes, is successfully secreted into extracellular milieu from Bacillus subtilis 168 under the direction of its native signal peptide (named SPPETase) |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
the enzyme can offer an important contribution towards a future sustainable closed loop plastic recycling industry |
| 3.1.1.101 | poly(ethylene terephthalate) hydrolase |
degradation |
the enzyme is a potential tool to solve the issue of polyester plastic pollution |
| 3.1.1.102 | mono(ethylene terephthalate) hydrolase |
degradation |
enzyme shows good activity against commercial bottle-derived PET, which is highly crystallized and is considerably active against PET film at low temperatures |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
degradation |
fungal glucuronoyl esterases (FGEs) catalyze cleavage of the ester bond connecting a lignin alcohol to the xylan-bound 4-O-methyl-D-glucuronic acid of glucuronoxylans. Thus, FGEs are capable of degrading lignin-carbohydrate complexes and have potential for biotechnological applications toward woody biomass utilization |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
degradation |
Glucuronoyl esterases (GEs) catalyze the cleavage of ester linkages found between lignin and glucuronic acid moieties on glucuronoxylan in plant biomass. As such, GEs represent promising biochemical tools in industrial processing of these recalcitrant resources |
 3.1.2.20 | acyl-CoA hydrolase |
degradation |
TEII can maintain effective polyketide biosynthesis by selectively removing the nonelongatable residues bound to acyl carrier proteins |
| 3.1.8.1 | aryldialkylphosphatase |
degradation |
the enzyme is used for the detoxification of organophosphate pesticides and realted chemical warfare agents such as VX and sarin |
| 3.1.8.1 | aryldialkylphosphatase |
degradation |
a series of substituted phenoxyalkyl pyridinium oximes enhance the degradation of surrogates of sarin (i.e. nitrophenyl isopropyl methylphosphonate, NIMP) and VX (i.e. nitrophenyl ethyl methylphosphonate, NEMP). Neither NIMP nor NEMP is hydrolyzed effectively by paraoxonase PON1 if one of these oximes is absent. In the presence of eight novel oximes, PON1-mediated degradation of both surrogates occurs |
| 3.1.8.1 | aryldialkylphosphatase |
degradation |
activity and stability of organophosphorus hydrolase are enhanced by interactions between the hydrophobic poly(propylene oxide) block of amphiphilic Pluronics and the enzyme. The strategy provides an efficient route to new formulations for decontaminating organophosphate neurotoxins |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
degradation |
- |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
degradation |
enzyme catalyse the hydrolysis of toxic organophosphorus cholinesterase-inhibiting compounds, including pesticides and chemical nerve agents |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
degradation |
approach to the use of enzyme encapsulated within liposomes, to protect against and treat chemical poisoning |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
degradation |
enzyme is capable of detoxifying chemical warfare agents by hydrolysis |
| 3.1.8.2 | diisopropyl-fluorophosphatase |
degradation |
use of enzyme for decomposition of soman in vitro |
| 3.1.13.1 | exoribonuclease II |
degradation |
RNA-binding domains of RNase II play a more important role in its exoribonuclease activity than they do in the activity of RNase R |
| 3.1.21.1 | deoxyribonuclease I |
degradation |
treatment of established 72 h biofilms with 100 microg per ml of DNase for 24 h induces incomplete Listeria monocytogenes biofilm dispersal, with about 25% biofilm remaining compared to control. Addition of proteinase K completely inhibits biofilm formation, and 72 h biofilms including those grown under stimulatory conditions are completely dispersed with 100 microg per ml proteinase K |
| 3.1.21.1 | deoxyribonuclease I |
degradation |
the degradation of extracellular DNA with enzymes such as DNase I is a rapid method to remove Campylobacter jejuni biofilms, and is likely to potentiate the activity of antimicrobial treatments and thus synergistically aid disinfection treatments |
| 3.2.1.4 | cellulase |
degradation |
cellulase is an industrially important enzyme for biomass saccharification at high temperature. beta-Glucan can be completely degraded to glucose at high temperature with a combination of the hyperthermophile Pyrococcus furiosus endocellulase (EGPf) and beta-glucosidase (BGLPf). beta-Glucans are polysaccharides of D-glucose monomers formed by beta(1->3),(1->4) mixed-linkage bonds. They occur most commonly as cellulose in plants, in the bran of cereal grains, the cell wall of baker's yeast, and in certain fungi, mushrooms, and bacteria |
| 3.2.1.4 | cellulase |
degradation |
a statistical optimization approach involving Plackett-Burman design and response surface methodology on submerged fermentation using cane molasses medium results in the production of 72410, 36420, 32420 and 5180 U/l of xylanase, endo-beta-1,4-glucanase, exo-beta-1,4-glucanase, and beta-glucosidase, respectively, i.e. more than fourfold improvements in production of xylanolytic and cellulolytic enzymes. Addition of microparticles engineers fungal morphology and enhances enzymes production. Maximum sugar yield of 578.12 and 421.79 mg/g substrate for waste tea cup and rice straw, respectively, are achieved after 24 h |
| 3.2.1.4 | cellulase |
degradation |
addition of Eg5A to cellobiase (i.e. cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, and the glucose release is 47% higher than with cellobiase treatment alone |
| 3.2.1.4 | cellulase |
degradation |
addition of isoform Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increasing saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than that cellobiase treatment alone |
| 3.2.1.4 | cellulase |
degradation |
after hydrolysis and fermentation of wheat straw a significant amount of active enzymes can be recovered by recycling the liquid phase. In the early stage of the process, enzyme adsorbs to the substrate, then gradually returning to the solution as the saccharification proceeds. The hydrolysis yield and enzyme recycling efficiency in consecutive recycling rounds can be increased by using high enzyme loadings and moderate temperatures. The amount of enzymes in the liquid phase increases with its thermostability and hydrolytic efficiency |
| 3.2.1.4 | cellulase |
degradation |
bioethanol production by Aspergillus fumigatus JCF at optimised growth conditions and Saccharomyces cerevisiae for simultaneous saccharification and fermentation. Using cotton seed as the substrate, maximum bioethanol concentration of 6.7 g/l can be achieved |
| 3.2.1.4 | cellulase |
degradation |
cellulase complex containing cellulolytic enzymes,endoglucanase CelE, EC 3.2.1.4, and beta-glucosidase BglA, EC 3.2.1.21, to completely degrade cellulose to glucose. The cellulases are displayed on the cell surface of Corynebacterium glutamicum by using themechanosensitive channel to anchor enzymes in the cytoplasmic membrane. The displayed cellulases complexes have a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0fold increase compared to the conversion by the secreted cellulases complexes. The displayed cellulases complexes increase the residual activities of cCelEand cBglA at 70°C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively |
| 3.2.1.4 | cellulase |
degradation |
during cultivation, consortium SV79 produces the maximum filter paper activity (FPase, 9.41 U/ml), carboxymethylcellulase activity (CMCase, 6.35 U/ml), and xylanase activity (4.28 U/ml) with sugarcane bagasse, spent mushroom substrate, and Sorbus anglica, respectively. The ethanol production using Miscanthus floridulus as substrate is up to 2.63 mM ethanol/g |
| 3.2.1.4 | cellulase |
degradation |
effect of nickel-cobaltite (NiCo2O4) nanoparticles on production and thermostability of the cellulase enzyme system. Maximum production of endoglucanase (211 IU/gds), beta-glucosidase (301 IU/gds), and xylanase (803 IU/gds) is achieved after 72 h without nanoparticles, while in the presence of 1 mM of nanoparticles, endoglucanase, beta-glucosidase, and xylanase activity increase by about 49, 53, and 19.8%, respectively, after 48 h of incubation. Crude enzyme is thermally stable for 7 h at 80°C in presence of nanoparticles, as against 4 h at the same temperature for control samples |
| 3.2.1.4 | cellulase |
degradation |
effects of microalgal biomass particle on the degree of enzymatic hydrolysis and bioethanol production by single enzyme hydrolysis (cellulase) and double enzyme hydrolysis (cellulase and cellobiase). The glucose yield from biomass in the smallest particle size range examined, i.e. 35 microm to 90 microm, is the highest, 134.73 mg glucose/g algae, while the yield from biomass in the larger particle size range from 295 microm to 425 microm is 75.45mg glucose/g algae. A similar trend is observed for bioethanol yield, with the highest yield of 0.47 g EtOH/g glucose obtained from biomass in the smallest particle size range |
| 3.2.1.4 | cellulase |
degradation |
enzyme extracts obtained from growing Acrophialophora nainiana on cellulose, dirty-cotton residue, sugarcane bagasse and banana stem can be used in the hydrolysis of sugarcane bagasse, untreated, pre-treated by steam explosion and pretreated by acid-catalysed steam explosion. The carbohydrase activity profile of the enzyme preparations varies significantly with the used carbon source. The highest enzyme activities, especially total cellulase (0.0132 IU) and xylanase (0.0774 IU) activities, are obtained with banana stem as the carbon source. On sugarcane bagasse, total cellulase activity on filter paper and pectinase activities are predominant. The exocellulase/endocellulase activity ratio (FPAsol/FPAinsol) of the cellulases produced varies between 1 and 4 depending on the substrate. The highest endocellulase activity (FPAinsol) content is obtained when grown on sugarcane bagasse |
| 3.2.1.4 | cellulase |
degradation |
hydrolysis of 2% carboxymethyl cellulose with purified enzyme at its optimum temperature and pH results in complete hydrolysis within 2 h yielding 18% cellotriose, 72% cellobiose and 10% glucose |
| 3.2.1.4 | cellulase |
degradation |
immobilization of enzyme on functionalized magnetic silica nanospheres using glutaraldehyde. Immobilized cellulase exhibits better resistance to high temperature and pH inactivation in comparison to free cellulase. Use of cross-linking agent leads to a greater amount of immobilized cellulase and better operational stability. The amount of immobilized cellulase with the cross-linking agent is 92 mg/g support. The activity of the immobilized cellulase is still 85.5% of the initial activity after 10 continuous uses |
| 3.2.1.4 | cellulase |
degradation |
mixtures of beta-xylosidase, xylanase, beta-glucosidase, and cellulase isolated from the metagenomic library of a long-term dry thermophilic methanogenic digester community retain high residual synergistic activities after incubation with cellulose, xylan, and steam-exploded corncob at 50°C for 72 h. About 55% dry weight of steam-exploded corncob is hydrolyzed to glucose and xylose by the synergistic action of the four enzymes at 50°C for 48 h |
| 3.2.1.4 | cellulase |
degradation |
preparation of functionalized magnetic nanospheres by co-condensation of tetraethylorthosilicate with aminosilanes 3-(2-aminoethylaminopropyl)-triethoxysilane (AEAPTES), 3-(2-aminoethy-laminopropyl)-trimethoxysilane (AEAPTMES) and 3-aminopropyltriethoxysilane (APTES) and use as supports for immobilization of cellulase. The magnetic nanospheres with core-shell morphologies exhibit higher capacity for cellulase immobilization than unfunctionalized magnetic nanospheres. AEAPTMES with methoxy groups is favored to be hydrolyzed and grafted on unfunctionalized magnetic nanospheres. AEAPTMES functionalized magnetic nanospheres with the highest zeta-potential (29 mV) exhibit 87% activity recovery, and the maximum amount of immobilized cellulase is112 mg/g support at concentration of initial cellulase of 8 mg/ml. Immobilized cellulase on AEAPTMES functionalized magnetic nanospheres has higher temperature stability and broader pH stability than other immobilized cellulases and free cellulase |
| 3.2.1.4 | cellulase |
degradation |
pretreatment method for lignocellulosic wheat straw to depolymerize lignin and expose the cellulose polymers to produce bioethanol. Wheat straw is pretreated with ligninolytic enzymes extract produced from Ganoderma lucidum under optimum solid state fermentation conditions. The pretreated biomass was further subjected to the enzymatic hydrolysis by crude unprocessed cellulases (beta-1,4-endoglucanase, 53.5 U/ml, beta-1,4-exoglucanase, 41.3 U/ml, beta-1,4-glucosidase, 46.8 U/ml, and xylanase 39 U/ml) produced by Trichoderma harzaianum. Under optimal conditions for enzymatic saccharification, 10% (w/v) of pretreated biomass is hydrolyzed completely and converted to 72.5 and 2.4 g/l of glucose and xylose, respectively |
| 3.2.1.4 | cellulase |
degradation |
saccharification of pretreated dry potato peels, carrot peels, composite waste mixture, orange peels, onion peels, banana peels, pineapple peels by crude enzyme extract from Aspergillus niger NS-2 results in cellulose conversion efficiencies of 9298% |
| 3.2.1.4 | cellulase |
degradation |
the purified enzyme decreases the viscosity of carboxymethyl cellulose when assessed at 70-85°C and is capable of releasing reducing sugars from acid-pretreated straw at 70 and 75°C |
| 3.2.1.4 | cellulase |
degradation |
Trichoderma reesei NRRL-6156 filter paper exocellulase and endocellulase hydrolysis of sugarcane bagasse, results in 224.0 and 229 gram of total reducing sugar per kilogram of dry bagasse at 43.4°C and a concentration of enzymatic extract of 18.6% in water and ultrasound baths, respectively. The yields obtained are comparable to commercial enzymes |
| 3.2.1.4 | cellulase |
degradation |
under simulated mashing conditions, addition of 60 U Egl5A reduces more viscosity (10.0 vs.7.6%) than 80 U of Ultraflo XL from Novozymes |
| 3.2.1.4 | cellulase |
degradation |
under simulated mashing conditions, addition of Cel7A (99 microg) reduces the mash viscosity by 9.1% and filtration time by 24.6% |
| 3.2.1.4 | cellulase |
degradation |
use of amine-functionalized cobalt ferrite (AF-CoFe2O4) magnetic nanoparticles for immobilization of cellulase. Particles show a mean diameter of about 8 nm and remain distinct with no significant change in size after binding with cellulase. The immobilized cellulase has higher thermal stability than free cellulase and shows good reusability after recovery |
| 3.2.1.4 | cellulase |
degradation |
use of mutant T57N/E53D/S79P/T80E/V101I/S133R/N155E/G189S/F191V/T233V/G239E/V265T/D271Y/G293A7S309W/S318P and previously engineered highly active, thermostable variants of the fungal cellobiohydrolases Cel6A and Cel7A to hydrolyzes cellulose synergistically at an optimum temperature of 70°C over 60 h.The thermostable mixture produces three times as much total sugar as the best mixture of the wild type enzymes operating at their optimum temperature of 60°C |
| 3.2.1.4 | cellulase |
degradation |
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities |
| 3.2.1.4 | cellulase |
degradation |
addition of recombinant Eg5A to cellobiase (cellobiohydrolase and beta-glucosidase) results in a 53% increase in saccharification of NaOH-pretreated barley straw, whereas the glucose release is 47% higher than with cellobiase treatment alone |
| 3.2.1.4 | cellulase |
degradation |
cellulase enzyme filtrate from Chaetomium thermophile saccharifies 5% kallar grass straw to 69% reducing sugars (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h |
| 3.2.1.4 | cellulase |
degradation |
comparison of endoglucanases able to rapidly reduce the viscosity of 15% (w/w, dry matter) hydrothermally pretreated wheat straw. Based on temperature profiling studies, Thermoascus aurantiacus EGII/Cel5A is the most promising enzyme for biomass liquefaction |
| 3.2.1.4 | cellulase |
degradation |
crude cellulase efficiently hydrolyzes office waste paper, algal pulp (Gracillaria verulosa), and biologically treated wheat straw at 60°C with sugar release of about 830 mg/ml, 285 mg/g, and 260 mg/g of the substrate, respectively |
| 3.2.1.4 | cellulase |
degradation |
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively |
| 3.2.1.4 | cellulase |
degradation |
Freeze-dried enzyme of Trichoderma reesei, even at higher enzyme concentration results in 60% reducing sugars yield (quantitatively) at 50°C. Glucose concentration in the hydrolysates from different fungi is in the decreasing order of Chaetomium thermophile > Trichoderma reesei > Sporotrichum thermophile > Aspergillus fumigatus > Torula thermophila > Humicola grisea > Malbranchea pulchella. At 60°C, thermostable enzymes hydrolyse kallar grass straw at a maximum rate for the initial 20 h |
| 3.2.1.4 | cellulase |
degradation |
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase |
| 3.2.1.4 | cellulase |
degradation |
oligosaccharides with degree of polymerization 2-10 are formed by hydrolysis of beta-glucan. The recombinant enzyme preparations are fast and effective in decreasing the reduced viscosity of wholegrain barley extract than some commercial enzyme preparations |
| 3.2.1.4 | cellulase |
degradation |
scale-up systems for cellulase production and enzymatic hydrolysis of pretreated rice straw at highsolid loadings and by Aspergillus terreus. In a horizontal rotary drum reactor at 50°C with 25 % (w/v) solid loading and 9 FPU/g substrate enzyme load up to 20 % highly concentrated fermentable sugars are obtained at 40 h with an increased saccharification efficiency of 76 % compared to laboratory findings (69.2 %). Nearly 79-84% of the cellulases and more than 90% of the sugars are recovered from the saccharification mixture |
| 3.2.1.4 | cellulase |
degradation |
use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 5.0, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase |
| 3.2.1.4 | cellulase |
degradation |
use of lucerne fibre as a cellulase-recycling vehicle during bioconversion processes. Adsorption of cellulase complexes is minimal at the pH optimum, 6.2, for fibre conversion to soluble sugars. Lowering of incubation temperature to 3°C enhances adsorption of fungal cellulases. The adsorptive capacity can be improved about 30% by raising the pH above the hydrolysis optimum during the recycling phase |
| 3.2.1.4 | cellulase |
degradation |
use to release dye in neutral pH conditions from indigo-dyed cotton-containing fabric in biostoning applications |
| 3.2.1.4 | cellulase |
degradation |
using enzymatic extract from M. thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively |
| 3.2.1.4 | cellulase |
degradation |
addition of Cel9K to a commercial enzyme set (Celluclast 1.5L + Novozym 188) increases the saccharification of the pretreated reed and rice straw powders by 30.4% and 15.9%, respectively |
| 3.2.1.4 | cellulase |
degradation |
enzyme releases high amounts of reducing sugars from wheat bran and corn cobs, being a useful biocatalyst for producing bioethanol and fine chemicals from agroresidues |
| 3.2.1.4 | cellulase |
degradation |
replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls |
| 3.2.1.4 | cellulase |
degradation |
under acidic conditions at 50°C, the enzyme is effective in digesting the green algae Ulva pertusa |
| 3.2.1.6 | endo-1,3(4)-beta-glucanase |
degradation |
oligosaccharides with degree of polymerization 2-10 are formed by hydrolysis of beta-glucan and laminarin. The recombinant enzyme preparations are fast and effective in decreasing the reduced viscosity of wholegrain barley extract than some commercial enzyme preparations |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
the substrate binding site of Xyn11A probably contains six subsites. Aromatic residues Tyr165, Trp9, Tyr69, Tyr80, Tyr65, Tyr88 and Tyr173 play an important role in the six subsites of Xyn11A |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
enzyme is able to degrade pulp and release substantial chromophoric materials and lignin derived compounds indicating its effective utility in pulp bleaching |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
Abf51A shows greater synergistic effect in combination with xylanase (2.92fold) on wheat arabinoxylan degradation than other reported enzymes, the amounts of arabinose, xylose, and xylobiose are all increased in comparison to that by the enzymes acting individually |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
agroresidues subjected to alkali and microwave irradiation for 6 min in order to expose the polysaccharide component to enzymatic hydrolysis lead to increased relase of sugars. The maximum sugar content is detected in the hydrolysate of microwave-irradiated wheat bran (6.20 mg/g substrate) followed by wheat straw (4.9 mg/g substrate) |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
co-immobilization of xylanase, beta-xylosidase and alpha-L-arabinofuranosidase from Penicillium janczewskii on a single support leads to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the alpha-L-arabinofuranosidase present high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
during degradation of bagasse, hemicellulose content, especially arabinan, and the cellulose crystallinity of bagasse affects the synergism of degrading enzymes cellulase and xylanase. Higher synergism (above 3.4) is observed for glucan conversion, at low levels of arabinan (0.9%), during the hydrolysis of peracetic acid pretreated bagasse. In contrast, 1-ethyl-3-methylimidazolium acetate pretreated bagasse shows lower cellulose crystallinity and achieves higher synergism (over 1.9) for xylan conversion. The combination of Thermobidfida endoglucanase Cel6A and xylanase Xyn11A results in higher synergism for glucan conversion than the combination of Cel6A with Clostridium thermocellum XynZ-C |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
hydrolysis of insoluble wheat arabinoxylan using different endoxylanases in combination with arabinofuranosidase Araf51A. The optimized combination is endoxylanases XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increases with the increase of Araf51A proportion in the enzyme mixture. Both free and enzymes immobilizedon commercial magnetic nanoparticles show a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes is retained, with 5.5fold increase in the production of sugars. A sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan is observed |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
immobilization of enzyme within calcium alginate beads using entrapment technique. Temperature (50°C) and pH (7.0) optima of immobilized enzyme remain same, but enzyme-substrate reaction time increases from 5.0 to 30.0 min as compared to free enzyme. The diffusion limit of high molecular weight xylan (corncob) causes a decline in Vmax of immobilized enzyme from 4773 to 203.7 U/min, whereas the Km value increases from 0.5074 to 0.5722 mg/ml. Immobilized endo-beta-1,4-xylanase is stable even at high temperatures and retains 18 and 9% residual activity at 70°C and 80°C, respectively. The immobilized enzyme also exhibits sufficient recycling efficiency up to five reaction cycles |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
immobilizazion of enzyme on various supports. Most active immobilized enzyme is achieved when Xyl2 is covalently bound to low functionalized agarose matrices, poorer activity is observed for Xyl2 immobilized on highly functionalized agarose or on nickel-affinity resin |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
pretreatments with alkali or acid significantly increase the relative release of pentose sugars, especially in alkali-pretreated canola meal (about 44%) and mustard bran (about 72%). The amounts of pentosan (g/100 g) in acid- and alkali-pretreated canola meal are 7.50 and 8.21 and in corresponding mustard bran are 8.67 and 10.39, respectively. These pretreated substrates produced a pentose content (g/100 g) of 2.10 in 18 h and 2.95 in 24 h, respectively, during hydrolysis. The main oligosaccharides in the hydrolyzates of alkali-pretreated substrates are xylo-glucuronic acid and xylobiose |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
the combination of Axy43A and Paenibacillus curdlanolyticus B-6 endo-xylanase Xyn10C greatly improves the efficiency of xylose and arabinose production from the highly substituted rye arabinoxylan |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
crude thermostable cellulases and xylanase hydrolyze phosphoric acid-swollen wheat straw, avicel and untreated xylan up to 74, 71 and 90 %, respectively |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
degradation of alpha-amylase-treated wheat bran by xylanase solubilises about 20% of the fibre residue, i.e. 10% of the original bran. Amylase, protease and xylanase treatments alter the composition of the original bran, removing starch (100%), a portion of the non-starch glucan (39%), xylan (57%), arabinan (61%), ash (62%) and other components including protein (52%). Pre-extraction of enzymatically-hydrolysable starch and xylan reduces the release of furfural. Steam explosion of the lignocellulosic residue followed by cellulase treatment and conversion to ethanol at a high substrate concentration (19%) gives an ethanol titre ofabout 25 g/l or a yield of 93% of the theoretical maximum |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
enzymatic treatment of kraft pulp with xylanase and laccase decreases the amount of chlorine needed for bleaching. Pretreatment of pulp followed by a chemical treatment with 3% NaOCl gives the same results as with chemicals at 7% NaOCl, resulting in 42% reduction in chlorine consumption |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
hydrolysis of pretreated Alfa fibers (Stipa tenacissima) by beta-D-glucosidase and xylanase, produced by a solid state fermentation process of wheat bran supplemented with lactose. The maximum saccharification yield of 83.23% is achieved under substrate concentration 3.7% (w/v), time 144 h and enzyme loading of 0.8 FPU, 15 U CMCase, 60 U beta-D-glucosidase and 125 U xylanase |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
maximum saccharification is obtained from treatment of cane bagasse by partially purified xylanase from Thermomyces lanuginosus A72 and Thermomyces lanuginosus YMN72 after 24 hrs of incubation. The maximum production of ethanol and xylitol is obtained after 48 and 24 h fermentation giving 22.48 g/l and 13.54 g/l, respectively, in enzyme broth of Thermomyces lanuginosus YMN72 using Candida tropicalis EMCC2 |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
optimization of xylanase production using agro-industrial substrates. Pretreated rice straw yields 126.9 mg/g maximum fermentable sugars |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
treatment of Eucalyptus kraft pulp with culture supernatant at 10 IU per gram pulp to enhance bleaching of kraft pulp results in a 10.5% reduction in Kappa number (indicating the amount of chemicals needed for bleaching pulps) and has a positive effect on the brightness of the resulting handsheets |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
using enzymatic extract from Myceliophthora thermophila JCP 1-4 to saccharify sugarcane bagasse pretreated with microwaves and glycerol, glucose and xylose yields obtained are 15.6% and 35.13% (2.2 g/l and 1.95 g/l), respectively |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
application in enzymatic hydrolysis for sugars production from lignocellulosic biomass. On empty fruit bunch as a feedstock, the total sugars conversion is 3.8%, and the conversion after alkaline pretreatment is approximately 16fold improved (61.1%) |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
application of enzyme for biobleaching of Eucalyptus kraft pulp, the xylanase increases the brightness of the pulp by 14.5% and reduces the kappa number by 24.5% |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
enzyme can be used for hydrolysis of pretreated agro-wastes. Sugarcane juice substituted medium yields maximum (52.19%) reducing sugar, followed by bioethanol production (4.19 g/l) at 72 h of incubation |
| 3.2.1.8 | endo-1,4-beta-xylanase |
degradation |
when a fusion protein with the carbohydrate-binding domain of xylanase XynZ from Clostridium thermocellum supplements the commercial cocktail Accellerase1 1500, reducing sugar release is improved by 17% from pretreated sugarcane bagasse |
| 3.2.1.11 | dextranase |
degradation |
crosslinking of dextranase on chitosan hydrogel microspheres. A shift in optimum pH and temperature from 7.0 to 7.5 and 50 to 60°C is observed after immobilization, respectively. Recycling efficiency, thermal stability, and activation energy distinctly improve after immobilization, whereas anchoring of substrate at the active site of the soluble dextranase exhibits an increase in Km with no change in Vmax after crosslinking |
